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Nat Commun ; 11(1): 5975, 2020 11 25.
Artigo em Inglês | MEDLINE | ID: mdl-33239621

RESUMO

Hop/Stip1/Sti1 is thought to be essential as a co-chaperone to facilitate substrate transfer between the Hsp70 and Hsp90 molecular chaperones. Despite this proposed key function for protein folding and maturation, it is not essential in a number of eukaryotes and bacteria lack an ortholog. We set out to identify and to characterize its eukaryote-specific function. Human cell lines and the budding yeast with deletions of the Hop/Sti1 gene display reduced proteasome activity due to inefficient capping of the core particle with regulatory particles. Unexpectedly, knock-out cells are more proficient at preventing protein aggregation and at promoting protein refolding. Without the restraint by Hop, a more efficient folding activity of the prokaryote-like Hsp70-Hsp90 complex, which can also be demonstrated in vitro, compensates for the proteasomal defect and ensures the proteostatic equilibrium. Thus, cells may act on the level and/or activity of Hop to shift the proteostatic balance between folding and degradation.


Assuntos
Proteínas de Choque Térmico HSP70/metabolismo , Proteínas de Choque Térmico HSP90/metabolismo , Proteínas de Choque Térmico/metabolismo , Proteínas de Saccharomyces cerevisiae/metabolismo , Células A549 , Técnicas de Inativação de Genes , Células HCT116 , Células HEK293 , Proteínas de Choque Térmico HSP90/genética , Proteínas de Choque Térmico/genética , Humanos , Mutagênese Sítio-Dirigida , Mutação , Complexo de Endopeptidases do Proteassoma/metabolismo , Agregados Proteicos , Dobramento de Proteína , Proteólise , Proteínas de Saccharomyces cerevisiae/genética
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